1b4d: Difference between revisions

Revision as of 18:13, 30 June 2008

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File:1b4d.png

Template:STRUCTURE 1b4d

AMIDOCARBAMATE INHIBITOR OF GLYCOGEN PHOSPHORYLASEAMIDOCARBAMATE INHIBITOR OF GLYCOGEN PHOSPHORYLASE

Template:ABSTRACT PUBMED 10211820

About this StructureAbout this Structure

1B4D is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

Effects of commonly used cryoprotectants on glycogen phosphorylase activity and structure., Tsitsanou KE, Oikonomakos NG, Zographos SE, Skamnaki VT, Gregoriou M, Watson KA, Johnson LN, Fleet GW, Protein Sci. 1999 Apr;8(4):741-9. PMID:10211820

Page seeded by OCA on Mon Jun 30 18:13:35 2008

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 {{STRUCTURE_1b4d|  PDB=1b4d  |  SCENE=  }}
-'''AMIDOCARBAMATE INHIBITOR OF GLYCOGEN PHOSPHORYLASE'''
+===AMIDOCARBAMATE INHIBITOR OF GLYCOGEN PHOSPHORYLASE===
-==Overview==
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-The effects of a number of cryoprotectants on the kinetic and structural properties of glycogen phosphorylase b have been investigated. Kinetic studies showed that glycerol, one of the most commonly used cryoprotectants in X-ray crystallographic studies, is a competitive inhibitor with respect to substrate glucose-1-P with an apparent Ki value of 3.8% (v/v). Cryogenic experiments, with the enzyme, have shown that glycerol binds at the catalytic site and competes with glucose analogues that bind at the catalytic site, thus preventing the formation of complexes. This necessitated a change in the conditions for cryoprotection in crystallographic binding experiments with glycogen phosphorylase. It was found that 2-methyl-2,4-pentanediol (MPD), polyethylene glycols (PEGs) of various molecular weights, and dimethyl sulfoxide (DMSO) activated glycogen phosphorylase b to different extents, by stabilizing its most active conformation, while sucrose acted as a noncompetitive inhibitor and ethylene glycol as an uncompetitive inhibitor with respect to glucose-1-P. A parallel experimental investigation by X-ray crystallography showed that, at 100 K, both MPD and DMSO do not bind at the catalytic site, do not induce any significant conformational change on the enzyme molecule, and hence, are more suitable cryoprotectants than glycerol for binding studies with glycogen phosphorylase.
+The line below this paragraph, {{ABSTRACT_PUBMED_10211820}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10211820}}
 ==About this Structure==
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 [[Category: Glycogen phosphorylase]]
 [[Category: Inhibitor binding]]
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